Qu L

References (10)

Title : Broad-Specificity Screening of Pyrethroids Enabled by the Catalytic Function of Human Serum Albumin on Coumarin Hydrolysis - Liang_2023_Anal.Chem__
Author(s) : Liang Z , Sun Y , Zeng H , Qin H , Yang R , Qu L , Zhang K , Li Z
Ref : Analytical Chemistry , : , 2023
Abstract : Sensing systems based on cholinesterase and carboxylesterase coupled with different transduction technologies have emerged for pesticide screening owing to their simple operation, fast response, and suitability for on-site analysis. However, the broad spectrum and specificity screening of pyrethroids over organophosphates and carbamates remains an unmet challenge for current enzymatic sensors. Human serum albumin (HSA), a multifunctional protein, can promote various chemical transformations and show a high affinity for pyrethroids, which offer a route for specific and broad-spectrum pyrethroid screening. Herein, for the first time, we evaluated the catalytic hydrolysis function of human serum albumin (HSA) on the coumarin lactone bond and revealed that HSA can act as an enzyme to catalyze the hydrolysis of the coumarin lactone bond. Molecular docking and chemical modifications indicate that lysine 199 and tyrosine 411 serve as the catalytic general base and contribute to most of the catalytic activity. Utilizing this enzymatic activity, a broad specific ratiometric fluorescence pyrethroids sensing system was developed. The binding energetics and binding constants of pesticides and HSA show that pyrethroids bind to HSA more easily than organophosphates and carbamates, which is responsible for the specificity of the sensing system. This study provides a general sensor platform and strategy for screening pesticides and reveals the catalytic activity of HSA on the hydrolysis of the coumarin lactone bond, which may open innovative horizons for the chemical sensing and biomedical applications of HSA.
ESTHER : Liang_2023_Anal.Chem__
PubMedSearch : Liang_2023_Anal.Chem__
PubMedID: 36952638

Title : Alcoholic Setdb1 suppression promotes hepatosteatosis in mice by strengthening Plin2 - Zhang_2023_Metabolism__155656
Author(s) : Zhang Y , Li Y , Liu Y , Wang H , Chen Y , Zhang B , Song M , Song L , Ding Q , Qiu J , Fan M , Qu L , Wang Z
Ref : Metabolism , :155656 , 2023
Abstract : BACKGROUND AND AIMS: Hepatosteatosis is one of the early features of alcoholic liver disease (ALD) and pharmaceutical or genetic interfering of the development of hepatosteatosis will efficiently alleviate the progression of ALD. Currently, the role of histone methyltransferase Setdb1 in ALD is not yet well understood. METHOD: Lieber-De Carli diet mice model and NIAAA mice model were constructed to confirm the expression of Setdb1. The hepatocyte-specific Setdb1-knockout (Setdb1-HKO) mice was established to determine the effects of Setdb1 in vivo. Adenovirus-Setdb1 were produced to rescue the hepatic steatosis in both Setdb1-HKO and Lieber-De Carli mice. The enrichment of H3k9me3 in the upstream sequence of Plin2 and the chaperone-mediated autophagy (CMA) of Plin2 were identified by ChIP and co-IP. Dual-luciferase reporter assay was used to detect the interaction of Setdb1 3'UTR and miR216b-5p in AML12 or HEK 293 T cells. RESULTS: We found that Setdb1 was downregulated in the liver of alcohol-fed mice. Setdb1 knockdown promoted lipid accumulation in AML12 hepatocytes. Meanwhile, hepatocyte-specific Setdb1-knockout (Setdb1-HKO) mice exhibited significant lipid accumulation in the liver. Overexpression of Setdb1 was performed with an adenoviral vector through tail vein injection, which ameliorated hepatosteatosis in both Setdb1-HKO and alcoholic diet-fed mice. Mechanistically, downregulated Setdb1 promoted the mRNA expression of Plin2 by desuppressing H3K9me3-mediated chromatin silencing in its upstream sequence. Pin2 acts as a critical membrane surface-associated protein to maintain lipid droplet stability and inhibit lipase degradation. The downregulation of Setdb1 also maintained the stability of Plin2 protein through inhibiting Plin2-recruited chaperone-mediated autophagy (CMA). To explore the reasons for Setdb1 suppression in ALD, we found that upregulated miR-216b-5p bound to the 3'UTR of Setdb1 mRNA, disturbed its mRNA stability, and eventually aggravated hepatic steatosis. CONCLUSIONS: Setdb1 suppression plays an important role in the progression of alcoholic hepatosteatosis via elevating the expression of Plin2 mRNA and maintaining the stability of Plin2 protein. Targeting hepatic Setdb1 might be a promising diagnostic or therapeutic strategy for ALD.
ESTHER : Zhang_2023_Metabolism__155656
PubMedSearch : Zhang_2023_Metabolism__155656
PubMedID: 37419179

Title : Screening the Degradation of Polymer Microparticles on a Chip - Davachi_2023_ACS.Omega_8_1710
Author(s) : Davachi SM , Mokhtare A , Torabi H , Enayati M , Deisenroth T , Van Pho T , Qu L , Tucking KS , Abbaspourrad A
Ref : ACS Omega , 8 :1710 , 2023
Abstract : Enzymatic degradation of polymers has advantages over standard degradation methods, such as soil burial and weathering, which are time-consuming and cannot provide time-resolved observations. We have developed a microfluidic device to study the degradation of single microparticles. The enzymatic degradation of poly (1,4-butylene adipate-co-terephthalate) (PBAT) microparticles was studied using Novozym 51032 cutinase. PBAT microparticles were prepared via an oil-in-water emulsion solvent removal method, and their morphology and chemical composition were characterized. Then, microparticles with varying diameters of 30-60 microm were loaded into the microfluidic chip. Enzyme solutions at different concentrations were introduced to the device, and changes in the size and transparency of PBAT microparticles were observed over time. The physicochemical properties of degraded products were analyzed by FT-IR, NMR, mass spectrometry, and differential scanning calorimetry. The degradation process was also performed in bulk, and the results were compared to those of the microfluidic method. Our analysis confirms that the degradation process in both bulk and microfluidic methods was similar. In both cases, degradation takes place on aliphatic and soft segments of PBAT. Our findings serve as a proof of concept for a microfluidic method for easy and time-resolved degradation analysis, with degradation results comparable to those of conventional bulk methods.
ESTHER : Davachi_2023_ACS.Omega_8_1710
PubMedSearch : Davachi_2023_ACS.Omega_8_1710
PubMedID: 36643556

Title : Highly selective SERS detection of acetylcholinesterase in human blood based on catalytic reaction - Chen_2022_Anal.Chim.Acta_1232_340495
Author(s) : Chen Y , Zhao W , Si J , Zheng Y , Tan H , Meng F , Yang G , Gu Y , Qu L
Ref : Anal Chim Acta , 1232 :340495 , 2022
Abstract : Acetylcholinesterase (AChE) is a key hydrolase in the cholinergic system, which directly determines the degradation of neurotransmitters. Therefore, it is a significant challenge to detect AChE in human blood with high sensitivity and selectivity in physiological and pathological processes. A novel nanoprobe by decorating the surface of gold nanoparticles with neostigmine (NE) AuNPs/NE was constructed for the AChE assay in serum. The principle is based on the specific recognition and cleavage of carbamate bonds in AuNPs/NE by AChE to form hydroxyl groups, resulting in changes of SERS spectra. The results show that 10 nm AuNPs/NE exhibit excellent catalytic activity for this reaction and the reaction rate is six times higher than that of 70 nm AuNPs/NE. Benefiting from the combined advantages of catalytic reaction specificity and molecular finger printing provided by SERS technology, AuNPs/NE exhibit high selectivity for AChE. The limit of detection (LOD) of this method for AChE activity was low to 0.02 U/mL. In addition, the spiked recovery of AChE in serum samples was 75.0%-119.2%. The proposed sensor also exhibits long-term stability and high biocompatibility with the increasing incubation time. More importantly, this work provides a new perspective for elucidating the role of AChE regulated by oxidative stress in the pathology of depression.
ESTHER : Chen_2022_Anal.Chim.Acta_1232_340495
PubMedSearch : Chen_2022_Anal.Chim.Acta_1232_340495
PubMedID: 36257753

Title : Acetylcholinesterase-Cu(3)(PO(4))(2) hybrid nanoflowers for electrochemical detection of dichlorvos using square-wave voltammetry - Yang_2022_Anal.Methods__
Author(s) : Yang L , Zhang X , Li M , Qu L , Liu Z
Ref : Anal Methods , : , 2022
Abstract : Immobilization of enzymes is one of the key steps in the development of high-performance enzymatic electrochemical biosensors, and various nanostructured materials have been designed and developed to achieve this goal. Herein, hybrid nanoflowers (HNFs) were synthesized using acetylcholinesterase (AChE) as an organic component and copper phosphate (Cu(3)(PO(4))(2)) as an inorganic component. These AChE-Cu(3)(PO(4))(2) HNFs exhibit a three-dimensional hierarchical flower-like structure, which not only has a large specific surface area but also promotes the affinity between AChE and its substrate with better catalytic activity. Not only that, the surface modification of the glassy carbon electrode (GCE) by the joint use of gold nanoparticles (AuNPs) and graphene oxide (GO) extended the electroactive area. Using square-wave voltammetry (SWV), the as-prepared biosensor (i.e., AChE-Cu(3)(PO(4))(2) HNF/AuNP/GO/GCE) demonstrated superior sensing performance in the detection of dichlorvos. The detection limit is as low as 0.07 pM, and the linear detection range can range from 0.5 pM to 10 microM. In addition, the biosensor was feasible in real agricultural samples with satisfactory recoveries (98.65% to 103.43%). The reported biosensor provides an alternative tool for the direct measurements of AChE activity and its inhibition. Besides organophosphorus pesticides represented by dichlorvos, this biosensor has the potential to detect other AChE inhibitors, such as carbamate pesticides, drugs for Alzheimer's disease, etc., thus having broader applications in food safety and drug screening.
ESTHER : Yang_2022_Anal.Methods__
PubMedSearch : Yang_2022_Anal.Methods__
PubMedID: 36169013

Title : An enzyme inhibition-based lab-in-a-syringe device for point-of-need determination of pesticides - Yang_2020_Analyst__
Author(s) : Yang L , Wang J , Qu L , Liu Z , Jiang L
Ref : Analyst , : , 2020
Abstract : An enzyme inhibition-based lab-in-a-syringe (EI-LIS) device was developed by integrating a 1-naphthol-linked bi-enzymatic reaction (sensor core) into the LIS (sensor device) for point-of-need monitoring of pesticide residues. The integration relies on the rational design of two reaction pads. The conjugate pad is a polyester fiber membrane loaded with plant-esterase, an alternative to acetylcholinesterase. Besides pesticide capture, plant-esterase also mediates the hydrolysis of 1-naphthyl acetate, generating 1-naphthol. The detection pad is an agarose gel entrapping oxidized 3,3',5,5'-tetramethylbenzidine (oxTMB) from Fe(iii) meso-tetra(N-methyl-4-pyridyl) porphyrin (FeTMPyP4)-catalyzed TMB oxidation. Both pads were embedded into their cartridges and then connected to a syringe. Under syringe pumping, 1-naphthol vertically flowed from the conjugate to the detection cartridge, linking the two pads. If plant-esterase was intact, 1-naphthol would reduce oxTMB, causing a color change of the detection pad from blue to colorless. If the plant-esterase activity was inhibited by pesticides, less 1-naphthol was produced, and the blue color of the detection pad would be partially or wholly retained. The deeper the blue color, the greater the pesticide concentration. This chromogenic pattern is responsible for a highly sensitive readout (detection limits of dichlorvos: 0.1 nM with the naked eye and 0.07 nM with a spectrometer).
ESTHER : Yang_2020_Analyst__
PubMedSearch : Yang_2020_Analyst__
PubMedID: 32319482

Title : Ambient light sensor based colorimetric dipstick reader for rapid monitoring organophosphate pesticides on a smart phone - Fu_2019_Anal.Chim.Acta_1092_126
Author(s) : Fu Q , Zhang C , Xie J , Li Z , Qu L , Cai X , Ouyang H , Song Y , Du D , Lin Y , Tang Y
Ref : Anal Chim Acta , 1092 :126 , 2019
Abstract : Organophosphate pesticides (OPs) are widely used around the world to control pests in agricultural, residential, and commercial settings. Ingestion of high-dose OPs could lead to acute toxicity, and persistent influence on health could result from acute poisoning or long-term exposure to low dose OPs. An easy to operate, low cost and home available OPs testing platform is urgently needed. Ambient light sensor (ALS) based smart phone colorimetric reader has the advantages of easy to operate, low cost, high accuracy and versatility. In this work, a novel ALS based smart phone colorimetric dipsticks (CDs) reader was reported for rapid monitoring OPs. In this method, acetylcholinesterase (ACHE) CDs was used to test OPs and results were analyzed using an ALS based reader according to the absorbance of ACHE CDs. The results obtained using the ALS based CDs reader were comparable to those obtained using gas chromatography-mass spectrometry (GC-MS) and Ellman assay. The ALS based CDs reader has the advantages of portable, low cost, and high accuracy, and therefore could act an effective platform for OPs monitoring.
ESTHER : Fu_2019_Anal.Chim.Acta_1092_126
PubMedSearch : Fu_2019_Anal.Chim.Acta_1092_126
PubMedID: 31708025

Title : HIF-1alpha up-regulates NDRG1 expression through binding to NDRG1 promoter, leading to proliferation of lung cancer A549 cells - Wang_2013_Mol.Biol.Rep_40_3723
Author(s) : Wang Q , Li LH , Gao GD , Wang G , Qu L , Li JG , Wang CM
Ref : Mol Biol Rep , 40 :3723 , 2013
Abstract : Hypoxia-inducible signaling pathway is involved in many pathological processes, such as adaptiveness regulation of plateau environment, myocardial ischemia and tumorigenesis. NDRG1 is a member of the N-myc downregulated gene (NDRG) family, and it has strong hypoxia stress reaction functions. Although the cellular responses to hypoxia are well known, little is known about the interaction between hypoxia-inducible transcription factor (HIF)-1alpha and NDRG1. In this study, we cloned HIF-1alpha CDS, NDRG1 promoter and its truncatures, constructed pCDNA3.0-Hif-1alpha and pGL3-basic-NDRG1. Reporter assay results showed that HIF-1alpha could bind to NDRG1 promoter to activate NDRG1 expression. Further results revealed that -1202 to -450 of NDRG1 promoter is the most important region for HIF-1alpha binding. Then, we constructed NDRG1 stable transfection cell line. Results from MTT, colony-forming assay and flow cytometry showed that NDRG1 overexpression results in more proliferation and less apoptosis of A549 lung cancer cells. Our study elucidates the mechanism of NGRG1 in hypoxia stress reactions and may provide new strategy for hypoxia injuries.
ESTHER : Wang_2013_Mol.Biol.Rep_40_3723
PubMedSearch : Wang_2013_Mol.Biol.Rep_40_3723
PubMedID: 23526365

Title : Dense genotyping of candidate gene loci identifies variants associated with high-density lipoprotein cholesterol - Edmondson_2011_Circ.Cardiovasc.Genet_4_145
Author(s) : Edmondson AC , Braund PS , Stylianou IM , Khera AV , Nelson CP , Wolfe ML , Derohannessian SL , Keating BJ , Qu L , He J , Tobin MD , Tomaszewski M , Baumert J , Klopp N , Doring A , Thorand B , Li M , Reilly MP , Koenig W , Samani NJ , Rader DJ
Ref : Circ Cardiovasc Genet , 4 :145 , 2011
Abstract : BACKGROUND: Plasma levels of high-density lipoprotein cholesterol (HDL-C) are known to be heritable, but only a fraction of the heritability is explained. We used a high-density genotyping array containing single-nucleotide polymorphisms (SNPs) from HDL-C candidate genes selected on known biology of HDL-C metabolism, mouse genetic studies, and human genetic association studies. SNP selection was based on tagging SNPs and included low-frequency nonsynonymous SNPs. METHODS AND
RESULTS: Association analysis in a cohort containing extremes of HDL-C (case-control, n=1733) provided a discovery phase, with replication in 3 additional populations for a total meta-analysis in 7857 individuals. We replicated the majority of loci identified through genome-wide association studies and present on the array (including ABCA1, APOA1/C3/A4/A5, APOB, APOE/C1/C2, CETP, CTCF-PRMT8, FADS1/2/3, GALNT2, LCAT, LILRA3, LIPC, LIPG, LPL, LRP4, SCARB1, TRIB1, ZNF664) and provide evidence that suggests an association in several previously unreported candidate gene loci (including ABCG1, GPR109A/B/81, NFKB1, PON1/2/3/4). There was evidence for multiple, independent association signals in 5 loci, including association with low-frequency nonsynonymous variants.
CONCLUSIONS: Genetic loci associated with HDL-C are likely to harbor multiple, independent causative variants, frequently with opposite effects on the HDL-C phenotype. Cohorts comprising subjects at the extremes of the HDL-C distribution may be efficiently used in a case-control discovery of quantitative traits.
ESTHER : Edmondson_2011_Circ.Cardiovasc.Genet_4_145
PubMedSearch : Edmondson_2011_Circ.Cardiovasc.Genet_4_145
PubMedID: 21303902
Gene_locus related to this paper: human-LIPG

Title : A genome-wide association study identifies LIPA as a susceptibility gene for coronary artery disease - Wild_2011_Circ.Cardiovasc.Genet_4_403
Author(s) : Wild PS , Zeller T , Schillert A , Szymczak S , Sinning CR , Deiseroth A , Schnabel RB , Lubos E , Keller T , Eleftheriadis MS , Bickel C , Rupprecht HJ , Wilde S , Rossmann H , Diemert P , Cupples LA , Perret C , Erdmann J , Stark K , Kleber ME , Epstein SE , Voight BF , Kuulasmaa K , Li M , Schafer AS , Klopp N , Braund PS , Sager HB , Demissie S , Proust C , Konig IR , Wichmann HE , Reinhard W , Hoffmann MM , Virtamo J , Burnett MS , Siscovick D , Wiklund PG , Qu L , El Mokthari NE , Thompson JR , Peters A , Smith AV , Yon E , Baumert J , Hengstenberg C , Marz W , Amouyel P , Devaney J , Schwartz SM , Saarela O , Mehta NN , Rubin D , Silander K , Hall AS , Ferrieres J , Harris TB , Melander O , Kee F , Hakonarson H , Schrezenmeir J , Gudnason V , Elosua R , Arveiler D , Evans A , Rader DJ , Illig T , Schreiber S , Bis JC , Altshuler D , Kavousi M , Witteman JC , Uitterlinden AG , Hofman A , Folsom AR , Barbalic M , Boerwinkle E , Kathiresan S , Reilly MP , O'Donnell CJ , Samani NJ , Schunkert H , Cambien F , Lackner KJ , Tiret L , Salomaa V , Munzel T , Ziegler A , Blankenberg S
Ref : Circ Cardiovasc Genet , 4 :403 , 2011
Abstract : BACKGROUND: eQTL analyses are important to improve the understanding of genetic association results. We performed a genome-wide association and global gene expression study to identify functionally relevant variants affecting the risk of coronary artery disease (CAD). METHODS AND RESULTS: In a genome-wide association analysis of 2078 CAD cases and 2953 control subjects, we identified 950 single-nucleotide polymorphisms (SNPs) that were associated with CAD at P<10(-3). Subsequent in silico and wet-laboratory replication stages and a final meta-analysis of 21 428 CAD cases and 38 361 control subjects revealed a novel association signal at chromosome 10q23.31 within the LIPA (lysosomal acid lipase A) gene (P=3.7x10(-8); odds ratio, 1.1; 95% confidence interval, 1.07 to 1.14). The association of this locus with global gene expression was assessed by genome-wide expression analyses in the monocyte transcriptome of 1494 individuals. The results showed a strong association of this locus with expression of the LIPA transcript (P=1.3x10(-96)). An assessment of LIPA SNPs and transcript with cardiovascular phenotypes revealed an association of LIPA transcript levels with impaired endothelial function (P=4.4x10(-3)). CONCLUSIONS: The use of data on genetic variants and the addition of data on global monocytic gene expression led to the identification of the novel functional CAD susceptibility locus LIPA, located on chromosome 10q23.31. The respective eSNPs associated with CAD strongly affect LIPA gene expression level, which was related to endothelial dysfunction, a precursor of CAD.
ESTHER : Wild_2011_Circ.Cardiovasc.Genet_4_403
PubMedSearch : Wild_2011_Circ.Cardiovasc.Genet_4_403
PubMedID: 21606135
Gene_locus related to this paper: human-LIPA